RecG protein: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 25: | Line 25: | ||
Additionally, the phosphodiester backbones of the duplex arms of the junction are interacting with Domain 1 and 3 of RecG. The interaction allows the formation of either a B-form (DNA) or an A-form duplex (DNA/RNA), what explains why RecG can unwind Holliday junctions (DNA) as well as R-loops (RNA)<ref>Singleton, M. R., Scaife, S. & Wigley, D. B. Structural analysis of DNA replication fork reversal by RecG. Cell 107, 79–89 (2001)</ref>. | Additionally, the phosphodiester backbones of the duplex arms of the junction are interacting with Domain 1 and 3 of RecG. The interaction allows the formation of either a B-form (DNA) or an A-form duplex (DNA/RNA), what explains why RecG can unwind Holliday junctions (DNA) as well as R-loops (RNA)<ref>Singleton, M. R., Scaife, S. & Wigley, D. B. Structural analysis of DNA replication fork reversal by RecG. Cell 107, 79–89 (2001)</ref>. | ||
'''FUNCTION''' | '''FUNCTION''' [[Image:Manganon2.jpg | thumb ]] | ||
RecG is an enzyme with helicase, translocase and ATPase activity. It binds to a stalled replication fork and converts it into a holliday junction, which can be resolved later by RuvC. | RecG is an enzyme with helicase, translocase and ATPase activity. It binds to a stalled replication fork and converts it into a holliday junction, which can be resolved later by RuvC. | ||
